3LK4

Crystal structure of CapZ bound to the uncapping motif from CD2AP

Summary for 3LK4

• Entry DOI: 10.2210/pdb3lk4/pdb
• Related: 3LK2 3LK3
• Descriptor: F-actin-capping protein subunit alpha-1, F-actin-capping protein subunit beta isoforms 1 and 2, CD2-associated protein, ... (4 entities in total)
• Functional Keywords: capz, cd2ap, actin filaments, uncapping, actin-filament regulators, protein-protein comple, actin capping, actin-binding, cytoplasm, cytoskeleton, protein binding
• Biological source: Gallus gallus (bantam,chickens); More
• Total number of polymer chains: 36
• Total formula weight: 811558.93

Authors

Hernandez-Valladares, M.,Kim, T.,Kannan, B.,Tung, A.,Cooper, J.A.,Robinson, R.C. (deposition date: 2010-01-27, release date: 2010-04-07, Last modification date: 2023-11-01)

Primary citation

Hernandez-Valladares, M.,Kim, T.,Kannan, B.,Tung, A.,Aguda, A.H.,Larsson, M.,Cooper, J.A.,Robinson, R.C.
Structural characterization of a capping protein interaction motif defines a family of actin filament regulators.
Nat.Struct.Mol.Biol., 17:497-503, 2010

PubMed Abstract: Capping protein (CP) regulates actin dynamics by binding the barbed ends of actin filaments. Removal of CP may be one means to harness actin polymerization for processes such as cell movement and endocytosis. Here we structurally and biochemically investigated a CP interaction (CPI) motif present in the otherwise unrelated proteins CARMIL and CD2AP. The CPI motif wraps around the stalk of the mushroom-shaped CP at a site distant from the actin-binding interface, which lies on the top of the mushroom cap. We propose that the CPI motif may act as an allosteric modulator, restricting CP to a low-affinity, filament-binding conformation. Structure-based sequence alignments extend the CPI motif-containing family to include CIN85, CKIP-1, CapZIP and a relatively uncharacterized protein, WASHCAP (FAM21). Peptides comprising these CPI motifs are able to inhibit CP and to uncap CP-bound actin filaments.

PubMed: 20357771
DOI: 10.1038/nsmb.1792

Experimental method

X-RAY DIFFRACTION (1.99 Å)